Comparative Large Scale Characterization of Plant versus Mammal Proteins Reveals Similar and Idiosyncratic N-α-Acetylation Features
Comparative Large Scale Characterization of Plant versus Mammal Proteins Reveals Similar and Idiosyncratic N-α-Acetylation Features
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DOI：
10.1074/mcp.m111.015131
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发表时间：
2012-06-01
影响因子：
7
通讯作者：
Giglione, Carmela
中科院分区：
文献类型：
--
作者：
Bienvenut, Willy V.;Sumpton, David;Giglione, Carmela
N-末端修饰在蛋白质的活性、稳定性或亚细胞区室化方面的命运中起主要作用。这种修饰在蛋白质组学研究中仍然描述不多，特征也很差，到目前为止，只有少数生物体之间的比较研究。该领域的最新进展现在允许在蛋白质组范围的质谱分析过程中富集和选择N-末端肽。这些有针对性的方法解开了蛋白质N-末端修饰的程度和性质。在这里，我们的目的是在模式植物拟南芥中研究这种修饰，以比较这些结果与从平行分析的人类样本中获得的结果。我们应用大规模分析来编译这两个数据集的可靠结论。我们的数据显示了特征修饰的强收敛性，特别是对于蛋白质N-末端甲硫氨酸切除，共翻译N-α-乙酰化，或动物和植物王国之间的N-肉豆蔻酰化。由于底物和N-α-乙酰化机制的趋同性，有可能鉴定出参与少数模型植物此类修饰的N-乙酰转移酶。最后，高比例的核编码的叶绿体蛋白质的特征是去除转运肽后成熟蛋白质的翻译后N-α-乙酰化。与动物不同，植物具有专门的途径，用于细胞器靶向蛋白的翻译后乙酰化。相应的机制尚未被发现。Molecular & Cellular Proteomics 11：10.1074/mcp.M111.015131，1-14，2012.
N-terminal modifications play a major role in the fate of proteins in terms of activity, stability, or subcellular compartmentalization. Such modifications remain poorly described and badly characterized in proteomic studies, and only a few comparison studies among organisms have been made available so far. Recent advances in the field now allow the enrichment and selection of N-terminal peptides in the course of proteome-wide mass spectrometry analyses. These targeted approaches unravel as a result the extent and nature of the protein N-terminal modifications. Here, we aimed at studying such modifications in the model plant Arabidopsis thaliana to compare these results with those obtained from a human sample analyzed in parallel. We applied large scale analysis to compile robust conclusions on both data sets. Our data show strong convergence of the characterized modifications especially for protein N-terminal methionine excision, co-translational N-alpha-acetylation, or N-myristoylation between animal and plant kingdoms. Because of the convergence of both the substrates and the N-alpha-acetylation machinery, it was possible to identify the N-acetyltransferases involved in such modifications for a small number of model plants. Finally, a high proportion of nuclear-encoded chloroplast proteins feature post-translational N-alpha-acetylation of the mature protein after removal of the transit peptide. Unlike animals, plants feature in a dedicated pathway for post-translational acetylation of organelle-targeted proteins. The corresponding machinery is yet to be discovered. Molecular & Cellular Proteomics 11: 10.1074/mcp.M111.015131, 1-14, 2012.